|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11720 |
PRK11720 |
UDP-glucose--hexose-1-phosphate uridylyltransferase; |
3-348 |
0e+00 |
|
UDP-glucose--hexose-1-phosphate uridylyltransferase;
Pssm-ID: 236963 [Multi-domain] Cd Length: 346 Bit Score: 629.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 3 TTFRASEHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPLTTVPRHDPHNPLCPGATRANGEVNPDYEGTFLFDNDFPA 82
Cdd:PRK11720 2 TQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 83 LQPDAPSPGPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCS 162
Cdd:PRK11720 82 LMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 163 NPHPHCQVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRHV 242
Cdd:PRK11720 162 NPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 243 RRLPELTPAERDDLSSIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGanwDHWQLHAHYYPPLLRSATVRKFMVGYEM 322
Cdd:PRK11720 242 LRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEEN---DHWQLHAHFYPPLLRSATVRKFMVGYEM 318
|
330 340
....*....|....*....|....*.
gi 83320115 323 LAQAQRDLTPEQAAERLRALPEVHYR 348
Cdd:PRK11720 319 LAETQRDLTAEQAAERLRAVSDIHYR 344
|
|
| GalT |
cd00608 |
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ... |
12-342 |
7.82e-175 |
|
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.
Pssm-ID: 238341 [Multi-domain] Cd Length: 329 Bit Score: 488.74 E-value: 7.82e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 12 HIRYNPLQDEWVLVSAHRMKRPWQGQVEhqPLTTVPRHDPHNPLCPGATRA-NGEVNPDYEgTFLFDNDFPALQPDAPSP 90
Cdd:cd00608 1 HRRYNPLTGEWVLVSPHRAKRPWQGQQE--APKKLPEYDPDCPLCPGNERAdTGEQNPDYD-VRVFENDFPALKPDAPAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 91 GPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHC 168
Cdd:cd00608 78 EDSDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 169 QVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRHVRRLPEL 248
Cdd:cd00608 158 QIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 249 TPAERDDLSSIMKKLLTKYDNLFETSFPYSMGWHGAPTGseaGANWDHWQLHAHYYPPLLRSATVRKFMVGYEMLA-QAQ 327
Cdd:cd00608 238 TDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFI 314
|
330
....*....|....*
gi 83320115 328 RDLTPEQAAERLRAL 342
Cdd:cd00608 315 NDVTPEQAAARLREV 329
|
|
| galT_1 |
TIGR00209 |
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ... |
2-348 |
2.50e-172 |
|
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]
Pssm-ID: 129313 [Multi-domain] Cd Length: 347 Bit Score: 483.31 E-value: 2.50e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 2 ATTFRASEHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPLTTVPRHDPHNPLCPGATRANGEVNPDYEGTFLFDNDFP 81
Cdd:TIGR00209 1 MTQFNPVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLPAYDPDCYLCPGNKRVTGDLNPDYTGTYVFTNDFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 82 ALQPDAPSPGPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGC 161
Cdd:TIGR00209 81 ALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 162 SNPHPHCQVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRH 241
Cdd:TIGR00209 161 SNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 242 VRRLPELTPAERDDLSSIMKKLLTKYDNLFETSFPYSMGWHGAPTGseaGANWDHWQLHAHYYPPLLRSATVRKFMVGYE 321
Cdd:TIGR00209 241 VLRITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPFN---GEENQHWQLHAHFYPPLLRSATVRKFMVGYE 317
|
330 340
....*....|....*....|....*..
gi 83320115 322 MLAQAQRDLTPEQAAERLRALPEVHYR 348
Cdd:TIGR00209 318 MLGETQRDLTAEQAAERLRALSDIHYR 344
|
|
| GalT |
COG1085 |
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism]; |
8-345 |
2.38e-157 |
|
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
Pssm-ID: 440702 [Multi-domain] Cd Length: 336 Bit Score: 444.66 E-value: 2.38e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 8 SEHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPltTVPRHDPHNPLCPGATRA-NGEVNPDYEGTFLFDNDFPALQPD 86
Cdd:COG1085 3 PDMPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPE--DPPEYDEDCPLCPGNERAtPPEIPPPGWDVRVFPNKFPALSPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 87 APsPGPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQ--YPWVQIFENKGAMMGCSNP 164
Cdd:COG1085 81 AP-DAREGDGLYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGASLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 165 HPHCQVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRHVRR 244
Cdd:COG1085 160 HPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 245 LPELTPAERDDLSSIMKKLLTKYDNLFETsFPYSMGWHGAPTGSEAGanwDHWQLHAHYYPPlLRSATVRKFMVGYEMLA 324
Cdd:COG1085 240 FEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPVDGEER---DHYHWHLEIYPR-LRSATVLKFLAGFELGA 314
|
330 340
....*....|....*....|..
gi 83320115 325 QA-QRDLTPEQAAERLRALPEV 345
Cdd:COG1085 315 GAfINDVTPEQAAERLREVSEV 336
|
|
| GalP_UDP_transf |
pfam01087 |
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ... |
4-177 |
1.32e-91 |
|
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.
Pssm-ID: 426039 [Multi-domain] Cd Length: 182 Bit Score: 271.86 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 4 TFRASEH---QHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPLTTVPRHDPHNPLCPGATRANGEVNPDYEGTFLFDNDF 80
Cdd:pfam01087 1 LFEETDHiylSHRRYNPLTGEWVLVSPHRLKRPWAGQQEKISKDTLPEYDPMCYLCPGPSRANGDFNPDYKSPFVFTNDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 81 PALQPDAPSPGP---SDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENK 155
Cdd:pfam01087 81 YALSKDNPYIKTdaiAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGAssYPKCVLCFENE 160
|
170 180
....*....|....*....|..
gi 83320115 156 GAMMGCSNPHPHCQVWASSFLP 177
Cdd:pfam01087 161 GYAMGCSNPHPHGQIWASSHLP 182
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11720 |
PRK11720 |
UDP-glucose--hexose-1-phosphate uridylyltransferase; |
3-348 |
0e+00 |
|
UDP-glucose--hexose-1-phosphate uridylyltransferase;
Pssm-ID: 236963 [Multi-domain] Cd Length: 346 Bit Score: 629.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 3 TTFRASEHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPLTTVPRHDPHNPLCPGATRANGEVNPDYEGTFLFDNDFPA 82
Cdd:PRK11720 2 TQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 83 LQPDAPSPGPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCS 162
Cdd:PRK11720 82 LMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 163 NPHPHCQVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRHV 242
Cdd:PRK11720 162 NPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 243 RRLPELTPAERDDLSSIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGanwDHWQLHAHYYPPLLRSATVRKFMVGYEM 322
Cdd:PRK11720 242 LRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEEN---DHWQLHAHFYPPLLRSATVRKFMVGYEM 318
|
330 340
....*....|....*....|....*.
gi 83320115 323 LAQAQRDLTPEQAAERLRALPEVHYR 348
Cdd:PRK11720 319 LAETQRDLTAEQAAERLRAVSDIHYR 344
|
|
| GalT |
cd00608 |
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ... |
12-342 |
7.82e-175 |
|
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.
Pssm-ID: 238341 [Multi-domain] Cd Length: 329 Bit Score: 488.74 E-value: 7.82e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 12 HIRYNPLQDEWVLVSAHRMKRPWQGQVEhqPLTTVPRHDPHNPLCPGATRA-NGEVNPDYEgTFLFDNDFPALQPDAPSP 90
Cdd:cd00608 1 HRRYNPLTGEWVLVSPHRAKRPWQGQQE--APKKLPEYDPDCPLCPGNERAdTGEQNPDYD-VRVFENDFPALKPDAPAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 91 GPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENKGAMMGCSNPHPHC 168
Cdd:cd00608 78 EDSDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 169 QVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRHVRRLPEL 248
Cdd:cd00608 158 QIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 249 TPAERDDLSSIMKKLLTKYDNLFETSFPYSMGWHGAPTGseaGANWDHWQLHAHYYPPLLRSATVRKFMVGYEMLA-QAQ 327
Cdd:cd00608 238 TDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFI 314
|
330
....*....|....*
gi 83320115 328 RDLTPEQAAERLRAL 342
Cdd:cd00608 315 NDVTPEQAAARLREV 329
|
|
| galT_1 |
TIGR00209 |
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ... |
2-348 |
2.50e-172 |
|
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]
Pssm-ID: 129313 [Multi-domain] Cd Length: 347 Bit Score: 483.31 E-value: 2.50e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 2 ATTFRASEHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPLTTVPRHDPHNPLCPGATRANGEVNPDYEGTFLFDNDFP 81
Cdd:TIGR00209 1 MTQFNPVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLPAYDPDCYLCPGNKRVTGDLNPDYTGTYVFTNDFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 82 ALQPDAPSPGPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGC 161
Cdd:TIGR00209 81 ALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 162 SNPHPHCQVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRH 241
Cdd:TIGR00209 161 SNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 242 VRRLPELTPAERDDLSSIMKKLLTKYDNLFETSFPYSMGWHGAPTGseaGANWDHWQLHAHYYPPLLRSATVRKFMVGYE 321
Cdd:TIGR00209 241 VLRITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPFN---GEENQHWQLHAHFYPPLLRSATVRKFMVGYE 317
|
330 340
....*....|....*....|....*..
gi 83320115 322 MLAQAQRDLTPEQAAERLRALPEVHYR 348
Cdd:TIGR00209 318 MLGETQRDLTAEQAAERLRALSDIHYR 344
|
|
| GalT |
COG1085 |
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism]; |
8-345 |
2.38e-157 |
|
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
Pssm-ID: 440702 [Multi-domain] Cd Length: 336 Bit Score: 444.66 E-value: 2.38e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 8 SEHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPltTVPRHDPHNPLCPGATRA-NGEVNPDYEGTFLFDNDFPALQPD 86
Cdd:COG1085 3 PDMPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPE--DPPEYDEDCPLCPGNERAtPPEIPPPGWDVRVFPNKFPALSPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 87 APsPGPSDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQ--YPWVQIFENKGAMMGCSNP 164
Cdd:COG1085 81 AP-DAREGDGLYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGASLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 165 HPHCQVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRHVRR 244
Cdd:COG1085 160 HPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHVSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 245 LPELTPAERDDLSSIMKKLLTKYDNLFETsFPYSMGWHGAPTGSEAGanwDHWQLHAHYYPPlLRSATVRKFMVGYEMLA 324
Cdd:COG1085 240 FEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPVDGEER---DHYHWHLEIYPR-LRSATVLKFLAGFELGA 314
|
330 340
....*....|....*....|..
gi 83320115 325 QA-QRDLTPEQAAERLRALPEV 345
Cdd:COG1085 315 GAfINDVTPEQAAERLREVSEV 336
|
|
| GalP_UDP_transf |
pfam01087 |
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ... |
4-177 |
1.32e-91 |
|
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.
Pssm-ID: 426039 [Multi-domain] Cd Length: 182 Bit Score: 271.86 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 4 TFRASEH---QHIRYNPLQDEWVLVSAHRMKRPWQGQVEHQPLTTVPRHDPHNPLCPGATRANGEVNPDYEGTFLFDNDF 80
Cdd:pfam01087 1 LFEETDHiylSHRRYNPLTGEWVLVSPHRLKRPWAGQQEKISKDTLPEYDPMCYLCPGPSRANGDFNPDYKSPFVFTNDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 81 PALQPDAPSPGP---SDHPLFQAEAAQGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENK 155
Cdd:pfam01087 81 YALSKDNPYIKTdaiAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGAssYPKCVLCFENE 160
|
170 180
....*....|....*....|..
gi 83320115 156 GAMMGCSNPHPHCQVWASSFLP 177
Cdd:pfam01087 161 GYAMGCSNPHPHGQIWASSHLP 182
|
|
| GalP_UDP_tr_C |
pfam02744 |
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ... |
183-351 |
2.66e-88 |
|
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.
Pssm-ID: 397044 [Multi-domain] Cd Length: 166 Bit Score: 263.19 E-value: 2.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 183 EERCQRAYQSQHGEPLLVEYGRQELLRKERLVLTSEHWLVLVPFWAVWPFQTLLLPRRHVRRLPELTPAERDDLSSIMKK 262
Cdd:pfam02744 1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 263 LLTKYDNLFETSFPYSMGWHGAPTGSEagaNWDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRAL 342
Cdd:pfam02744 81 LTRRYDNLFETSFPYSMGIHQAPLNAE---ELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRAL 157
|
....*....
gi 83320115 343 PEVHYRLGQ 351
Cdd:pfam02744 158 SEVHYRWAL 166
|
|
| PLN02643 |
PLN02643 |
ADP-glucose phosphorylase |
13-299 |
1.50e-26 |
|
ADP-glucose phosphorylase
Pssm-ID: 215346 [Multi-domain] Cd Length: 336 Bit Score: 107.92 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 13 IRYNPLQDEWVLVSAHRMKRPwQGQVEHQPLTTVPRHDPHNPLCPGATRANG-EV--------NPDYEgTFLFDNDFPAL 83
Cdd:PLN02643 4 LRKDPVTNRWVIFSPARGKRP-TDFKSKSPQNPNGNHSSGCPFCIGHEHECApEIfrvpddasAPDWK-VRVIENLYPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 84 QPDAPSPGPSDHPLFQAEAAQ---GVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGA--QYPWVQIFENKGAM 158
Cdd:PLN02643 82 SRDLEPPCTEGQGEDYGGRRLpgfGFHDVVIETPVHSVQLSDLPARHIGEVLKAYKKRINQLQSdsRFKYVQVFKNHGAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 159 MGCSNPHPHCQVWASSFLPDVAQREERCQRAYQSQHGEPLLVEYGRQELLRKErlvltSEHWLVLVPFWAVWPFQTLLLP 238
Cdd:PLN02643 162 AGASMSHSHSQIIALPVVPPSVSARLDGSKEYFEKTGKCSLCEVVKKDLLIDE-----SSHFVSIAPFAATFPFEIWIIP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83320115 239 RRHVRRLPELTPAERDDLSSIMKKLLTKYDNLFETSfPYSMGWHGAPTG-SEAGANWDHWQL 299
Cdd:PLN02643 237 RDHSSNFHEIDDDKAVDLGGLLKLMLQKISKQLNDP-PYNYMIQTSPLGvEESNLPYTHWFL 297
|
|
| HIT_like |
cd00468 |
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ... |
67-172 |
1.12e-08 |
|
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups.
Pssm-ID: 238263 [Multi-domain] Cd Length: 86 Bit Score: 51.70 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 67 NPDYEGTFLFDNDFPAlqpdapspgpsdhplfqaeaaQGVCKVMCFHPWSDvTLPLMSVPEIRAVVDAWASVTEEL--GA 144
Cdd:cd00468 1 VPDDEHSFAFVNLKPA---------------------APGHVLVCPKRHVE-TLPDLDEALLADLVITAQRVAAELekHG 58
|
90 100
....*....|....*....|....*...
gi 83320115 145 QYPWVQIFENKGAMMGCSNPHPHCQVWA 172
Cdd:cd00468 59 NVPSLTVFVNDGAAAGQSVPHVHLHVLP 86
|
|
| HinT |
COG0537 |
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ... |
234-341 |
3.33e-03 |
|
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only];
Pssm-ID: 440303 [Multi-domain] Cd Length: 133 Bit Score: 37.24 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83320115 234 TLLLPRRHVRRLPELTPAERDDLSSIMKKLLTKYDNLFETSfPYSMGWHgapTGSEAGANWDHwqLHAHYYPpllRSATV 313
Cdd:COG0537 38 TLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPD-GFNLGIN---NGEAAGQTVPH--LHVHVIP---RYEGD 108
|
90 100
....*....|....*....|....*...
gi 83320115 314 RKFMVGYEMLAQAQRdltPEQAAERLRA 341
Cdd:COG0537 109 DNFMPVIGTKVDPEE---LEETARKLRA 133
|
|
| PRK14109 |
PRK14109 |
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase] ... |
278-342 |
7.54e-03 |
|
bifunctional [glutamine synthetase] adenylyltransferase/[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase;
Pssm-ID: 237613 [Multi-domain] Cd Length: 1007 Bit Score: 38.29 E-value: 7.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83320115 278 SMGWHGAPTGSEAGANWDHWQLHAH---------YYPPLLrSATVRkfmvgyemLAQAQRDLTPEQAAERLRAL 342
Cdd:PRK14109 464 AAGLRPDGRRDAAEELRAEWRRTRRrvrrlheklFYRPLL-EAVAR--------LSAEEARLSPEAARRRLAAL 528
|
|
| |
